Changes in Human Immunodeficiency Virus Type 1 Gag at Positions L449 and P453 Are Linked to I50V Protease Mutants In Vivo and Cause Reduction of Sensitivity to Amprenavir and Improved Viral Fitness In Vitro
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creator | Maguire, Michael F Guinea, Rosario Griffin, Philip Macmanus, Sarah Elston, Robert C Wolfram, Josie Richards, Naomi Hanlon, Mary H Porter, David J T Wrin, Terri Parkin, Neil Tisdale, Margaret Furfine, Eric Petropoulos, Chris Snowden, B Wendy Kleim, Jörg-Peter |
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</description><identifier>ISSN: 0022-538X</identifier><identifier>EISSN: 1098-5514</identifier><identifier>DOI: 10.1128/JVI.76.15.7398-7406.2002</identifier><identifier>PMID: 12097552</identifier><language>eng</language><publisher>United States: American Society for Microbiology</publisher><subject>Binding Sites ; Carbamates ; Drug Resistance, Viral ; Drug Therapy, Combination ; gag Gene Products, Human Immunodeficiency Virus ; Gene Products, gag - chemistry ; Gene Products, gag - genetics ; Gene Products, gag - metabolism ; HIV Protease - genetics ; HIV Protease - metabolism ; HIV Protease Inhibitors - pharmacology ; HIV Protease Inhibitors - therapeutic use ; HIV-1 - drug effects ; HIV-1 - enzymology ; HIV-1 - physiology ; Humans ; Microbial Sensitivity Tests ; Mutation ; Substrate Specificity ; Sulfonamides - pharmacology ; Sulfonamides - therapeutic use ; Vaccines and Antiviral Agents ; Virus Replication</subject><ispartof>Journal of Virology, 2002-08, Vol.76 (15), p.7398-7406</ispartof><rights>Copyright © 2002, American Society for Microbiology 2002</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4542-1b263d6f67c467bbe74b40cfd954889deb7505b3f0e02be804935b6657d776ba3</citedby><cites>FETCH-LOGICAL-c4542-1b263d6f67c467bbe74b40cfd954889deb7505b3f0e02be804935b6657d776ba3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC136352/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC136352/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12097552$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Maguire, Michael F</creatorcontrib><creatorcontrib>Guinea, Rosario</creatorcontrib><creatorcontrib>Griffin, Philip</creatorcontrib><creatorcontrib>Macmanus, Sarah</creatorcontrib><creatorcontrib>Elston, Robert C</creatorcontrib><creatorcontrib>Wolfram, Josie</creatorcontrib><creatorcontrib>Richards, Naomi</creatorcontrib><creatorcontrib>Hanlon, Mary H</creatorcontrib><creatorcontrib>Porter, David J T</creatorcontrib><creatorcontrib>Wrin, Terri</creatorcontrib><creatorcontrib>Parkin, Neil</creatorcontrib><creatorcontrib>Tisdale, Margaret</creatorcontrib><creatorcontrib>Furfine, Eric</creatorcontrib><creatorcontrib>Petropoulos, Chris</creatorcontrib><creatorcontrib>Snowden, B Wendy</creatorcontrib><creatorcontrib>Kleim, Jörg-Peter</creatorcontrib><title>Changes in Human Immunodeficiency Virus Type 1 Gag at Positions L449 and P453 Are Linked to I50V Protease Mutants In Vivo and Cause Reduction of Sensitivity to Amprenavir and Improved Viral Fitness In Vitro</title><title>Journal of Virology</title><addtitle>J Virol</addtitle><description>Article Usage Stats
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</description><subject>Binding Sites</subject><subject>Carbamates</subject><subject>Drug Resistance, Viral</subject><subject>Drug Therapy, Combination</subject><subject>gag Gene Products, Human Immunodeficiency Virus</subject><subject>Gene Products, gag - chemistry</subject><subject>Gene Products, gag - genetics</subject><subject>Gene Products, gag - metabolism</subject><subject>HIV Protease - genetics</subject><subject>HIV Protease - metabolism</subject><subject>HIV Protease Inhibitors - pharmacology</subject><subject>HIV Protease Inhibitors - therapeutic use</subject><subject>HIV-1 - drug effects</subject><subject>HIV-1 - enzymology</subject><subject>HIV-1 - physiology</subject><subject>Humans</subject><subject>Microbial Sensitivity Tests</subject><subject>Mutation</subject><subject>Substrate Specificity</subject><subject>Sulfonamides - pharmacology</subject><subject>Sulfonamides - therapeutic use</subject><subject>Vaccines and Antiviral Agents</subject><subject>Virus Replication</subject><issn>0022-538X</issn><issn>1098-5514</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFks2O0zAUhSMEYsrAK6ArFuxa7MQ_yYJFVTEzQUVUMFTsLCe5aT00dsdOivqSPBPOtIJhxcryved8Olc6SQKUzChN83cf1-VMihnlM5kV-VQyImYpIemTZEJJHHBO2dNkEifplGf594vkRQh3hFDGBHueXNCUFJLzdJL8Wmy13WAAY-Fm6LSFsusG6xpsTW3Q1kdYGz8EuD3uEShc6w3oHlYumN44G2DJWAHaNrBiPIO5R1ga-wMb6B2UnKxh5V2POiB8Gnpt-wCljciDezAt9BA3X7AZ6hEHroWvaEf2wfTHkTHv9h6tPhj_YCjj1x0iPqbSO7gyvcVwZvbevUyetXoX8NX5vUy-XX24XdxMl5-vy8V8Oa0ZZ-mUVqnIGtEKWTMhqwolqxip26bgLM-LBivJCa-yliBJK8wJKzJeCcFlI6WodHaZvD9x90PVYVOj7WMctfem0_6onDbq3401W7VxB0UzkfE0-t-e_d7dDxh61ZlQ426nLbohKElzyYri_0KaM57LgkRhfhLW3oXgsf0ThhI1lkbF0igpFOVqLI0aS6PG0kTr68fH_DWeWxIFb06CrdlsfxqPSodO3R3MI172G6kfy2o</recordid><startdate>20020801</startdate><enddate>20020801</enddate><creator>Maguire, Michael F</creator><creator>Guinea, Rosario</creator><creator>Griffin, Philip</creator><creator>Macmanus, Sarah</creator><creator>Elston, Robert C</creator><creator>Wolfram, Josie</creator><creator>Richards, Naomi</creator><creator>Hanlon, Mary H</creator><creator>Porter, David J T</creator><creator>Wrin, Terri</creator><creator>Parkin, Neil</creator><creator>Tisdale, Margaret</creator><creator>Furfine, Eric</creator><creator>Petropoulos, Chris</creator><creator>Snowden, B Wendy</creator><creator>Kleim, Jörg-Peter</creator><general>American Society for Microbiology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7U9</scope><scope>H94</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020801</creationdate><title>Changes in Human Immunodeficiency Virus Type 1 Gag at Positions L449 and P453 Are Linked to I50V Protease Mutants In Vivo and Cause Reduction of Sensitivity to Amprenavir and Improved Viral Fitness In Vitro</title><author>Maguire, Michael F ; 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</abstract><cop>United States</cop><pub>American Society for Microbiology</pub><pmid>12097552</pmid><doi>10.1128/JVI.76.15.7398-7406.2002</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Binding Sites Carbamates Drug Resistance, Viral Drug Therapy, Combination gag Gene Products, Human Immunodeficiency Virus Gene Products, gag - chemistry Gene Products, gag - genetics Gene Products, gag - metabolism HIV Protease - genetics HIV Protease - metabolism HIV Protease Inhibitors - pharmacology HIV Protease Inhibitors - therapeutic use HIV-1 - drug effects HIV-1 - enzymology HIV-1 - physiology Humans Microbial Sensitivity Tests Mutation Substrate Specificity Sulfonamides - pharmacology Sulfonamides - therapeutic use Vaccines and Antiviral Agents Virus Replication |
title | Changes in Human Immunodeficiency Virus Type 1 Gag at Positions L449 and P453 Are Linked to I50V Protease Mutants In Vivo and Cause Reduction of Sensitivity to Amprenavir and Improved Viral Fitness In Vitro |
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